Archer VariantPlex
p53 Kit


Having a technically strong NGS panel with simple and consistent library preparation is critical for variant detection. The Archer® VariantPlex® p53 Kit combines superior TP53 gene coverage with robust enrichment chemistry and an easy-to-use workflow to give you confident, sensitive and quantitative TP53 variant calling.


  • Superior TP53 coverage - ensures that variants are not missed due to lack of coverage
  • Molecular barcodes - Anchored Multiplex PCR (AMP™) enrichment chemistry enables unique molecule counting and provides an accurate measure of library complexity for confident sample sensitivity
  • Simple, lyophilized workflow - serial transfers and lyophilized reagents reduce hands on time and minimize consistency issues between libraries
  • Powerful analysis - Archer Analysis software detects germline and somatic variants and provides embedded mutation visualization and variant effect prediction

For Research Use Only. Not for use in diagnostic procedures. For Research Use Only. Not for use in diagnostic procedures.

Product information


SK0069-ILMN-8 - 8-reactions
SK0069-ILMN-16 - 16-reactions - starter kit

Archer Analysis

Local installation
Analysis Unlimited

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Specifications and performance


# of GSP2s


Total target size


Input DNA required


Recommended # of reads


Coverage uniformity > 20% mean

2.5 hours

Hands-on time

9.5 hours

Total time



Fresh frozen or FFPE

Sample types

†Coverage uniformity and recommended number of reads expected.
‡input recommendations for FFPE samples varies depending on Archer Preseq® DNA QC score. 50ng input recommended in absence of PreSeq screening

Gene targets


Need to modify this panel?

Add any of our wet lab-validated designs to this panel with Archer Assay Designer to build an assay that fits your exact requirements.

Tumor protein p53 function

Tumor protein p53 is encoded by the TP53 gene, which contains 12 coding exons and is located on the short arm of chromosome 17 at position 13.1. p53 contains transcriptional activation, DNA binding, and oligomerization domains. The protein regulates the cell cycle and maintains genomic stability through many different mechanisms of action. The protein is localized in the nucleus where it functions as a transciption factor.

When DNA damage occurs due to radiation, ultra-violet light, genotoxic drugs, nutrition deprivation, or heat/cold shock, p53 is activated via the ATM-CHK2 or ATR-CHK1 DNA repair pathways. Cell nutrition deprivation and heat/cold shock can stimulate p53 directly through hypoxia and the subsequent production of nitric oxide. Once stimulated, p53 transctiptionally activates target genes (1,2). The target genes can induce apoptosis, senescence, DNA repair, changes in metabolism, and cell cycle arrest. One p53 effector, p21, is a potent negative regulator of cell cycle progression and cell division, and its up regulation results in cell cycle arrest. Pausing the cell cycle gives the cell the opportunity to make repairs, if possible, or commit to p53-mediated cell death.

p53 mutations in cancer

Loss of p53 function through genetic mutations or disturbances in the p53-signaling pathway is a common feature in cancers. In fact, according to the International Cancer Genome Consortium, the TP53 gene is mutated in the majority of ovarian, esophageal, lung, rectal, pancreatic, oral, colon, and brain cancers. Greater than 75% of TP53 mutations result in expression of a mutant p53 protein that has lost some level of wild-type function (3). Impaired p53 can inhibit downstream tumor suppression, resulting in uncontrolled neoplastic growth. p53 has been shown to gain oncogenic functions from genetic mutations in the TP53 gene (4). The tumor-driving functions of mutant p53 include angiogenesis, stem cell expansion, survival, proliferation, enhanced chemo-resistance, mitogenic defects, metastasis, migration, and genomic instability (5-8).

p53 tumor supressor protein


  1. Kanehisa M, Goto S. KEGG: Kyoto encyclopedia of genes and genomes. Nucleic Acids res. 2000;28(1):27-30.
  2. Kanehisa M, Goto S, Sato Y, Kawashima M, Furumichi M, Tanabe M. Data, information, knowledge and principle: back to metabolism in KEGG. Nucleic Acids Res. 2014;42(Database issue):D199-D205. doi:10.1093/nar/gkt1076.
  3. Petitjean A, Mathe E, Kato S, et al. Impact of mutant p53 functional properties on TP53 mutation patterns and tumor phenotype: lessons from recent developments in the IARC TP53 database. Hum Mutat. 2007;28(6):622-629. doi:10.1002/humu.20495.
  4. Strano S, Dell'Orso S, Mongiovi AM, et al. Mutant p53 proteins: between loss and gain of function. Head Neck. 2007;29(5):488-496. doi:10.1002/hed.20531.
  5. Liu DP, Song H, Xu Y. A common gain of function of p53 cancer mutants in inducing genetic instability. Oncogene. 2010;29(7):949-956. doi:10.1038/onc.2009.376.
  6. Lang GA, Iwakuma T, Suh Y-A, et al. Gain of function of a p53 hot spot mutation in a mouse model of Li-Fraumeni syndrome. Cell. 2004;119(6):861-872.
  7. Oliv KP, Tuveson DA, Ruhe ZC, et al. Mutant p53 gain of function in two mouse models of Li-Fraumeni syndrome. Cell. 2004;119(6):847-860. doi:10.1016/j.cell.2004.11.004.
  8. Muller PAJ, Vousdan KH. p53 mutations in cancer. Nat Cell Biol. 2013;15(1):2-8. doi:10.1038/ncb2641.

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How to contact us


2477 55th Street, Suite 202

Boulder, CO 80301


Phone: (877) 771 1093

Phone: (303) 357 9001

All content © 2018 ArcherDX, Inc.

For Research Use Only. Not for use in diagnostic procedures. For Research Use Only. Not for use in diagnostic procedures.